HIS4_METVA
ID HIS4_METVA Reviewed; 238 AA.
AC P05324;
DT 01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1988, sequence version 1.
DT 25-MAY-2022, entry version 102.
DE RecName: Full=1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase;
DE EC=5.3.1.16;
DE AltName: Full=Phosphoribosylformimino-5-aminoimidazole carboxamide ribotide isomerase;
GN Name=hisA;
OS Methanococcus vannielii.
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanococcaceae; Methanococcus.
OX NCBI_TaxID=2187;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3923489; DOI=10.1073/pnas.82.12.4207;
RA Cue D., Beckler G.S., Reeve J.N., Konisky J.;
RT "Structure and sequence divergence of two archaebacterial genes.";
RL Proc. Natl. Acad. Sci. U.S.A. 82:4207-4211(1985).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-52.
RX PubMed=2829115; DOI=10.1093/nar/16.1.135;
RA Brown J.W., Thomm M., Beckler G.S., Frey G., Stetter K.O., Reeve J.N.;
RT "An archaebacterial RNA polymerase binding site and transcription
RT initiation of the hisA gene in Methanococcus vannielii.";
RL Nucleic Acids Res. 16:135-150(1988).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-(5-phospho-beta-D-ribosyl)-5-[(5-phospho-beta-D-
CC ribosylamino)methylideneamino]imidazole-4-carboxamide = 5-[(5-
CC phospho-1-deoxy-D-ribulos-1-ylimino)methylamino]-1-(5-phospho-beta-D-
CC ribosyl)imidazole-4-carboxamide; Xref=Rhea:RHEA:15469,
CC ChEBI:CHEBI:58435, ChEBI:CHEBI:58525; EC=5.3.1.16;
CC -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine
CC from 5-phospho-alpha-D-ribose 1-diphosphate: step 4/9.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the HisA/HisF family. {ECO:0000305}.
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DR EMBL; M11219; AAA72490.1; -; Genomic_DNA.
DR EMBL; X07391; CAA30300.1; -; Genomic_DNA.
DR PIR; S00580; S00580.
DR PIR; T48888; T48888.
DR AlphaFoldDB; P05324; -.
DR SMR; P05324; -.
DR UniPathway; UPA00031; UER00009.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0003949; F:1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino]imidazole-4-carboxamide isomerase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0000105; P:histidine biosynthetic process; IEA:UniProtKB-UniRule.
DR CDD; cd04732; HisA; 1.
DR Gene3D; 3.20.20.70; -; 1.
DR HAMAP; MF_01014; HisA; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR006062; His_biosynth.
DR InterPro; IPR006063; HisA_bact_arch.
DR InterPro; IPR044524; Isoase_HisA-like.
DR InterPro; IPR023016; Isoase_HisA-like_bact.
DR InterPro; IPR011060; RibuloseP-bd_barrel.
DR PANTHER; PTHR43090; PTHR43090; 1.
DR Pfam; PF00977; His_biosynth; 1.
DR SUPFAM; SSF51366; SSF51366; 1.
DR TIGRFAMs; TIGR00007; TIGR00007; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis; Cytoplasm; Histidine biosynthesis; Isomerase.
FT CHAIN 1..238
FT /note="1-(5-phosphoribosyl)-5-[(5-
FT phosphoribosylamino)methylideneamino] imidazole-4-
FT carboxamide isomerase"
FT /id="PRO_0000142098"
FT ACT_SITE 8
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT ACT_SITE 130
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT CONFLICT 26
FT /note="H -> Q (in Ref. 2; CAA30300)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 238 AA; 25712 MW; 5082D2AF54D9E756 CRC64;
MLIIPAVDMK NKKCVQLIQG NPDKKHVELD NPPEIAKKWV EQGAEMLHLV NLDGAINGKR
VNDEFIEETI KNSGVPVQIG GGIRSVSDAL YFIEKGAEKV ILGTVAIQNP KIVREISSIV
GKEKVTVALD AKDGKVLIKG WTEKTDYSPV QIGKILENMG AGSILFTNVD SEGLLEGINV
LPTKELVDNL NIPIIASGGV TTVEDLLKFK EIGVYAVVVG SALYKDMINL KDAILASK
